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Related Concept Videos

Herpes01:28

Herpes

Herpes simplex type 1 (HSV‑1) is a widespread pathogen responsible for orolabial lesions. It is an enveloped, double-stranded DNA (dsDNA) virus belonging to the family Herpesviridae. Once the virus infects a host cell, its double‑stranded DNA genome is delivered into the nucleus, where a coordinated cascade of immediate‑early, early, and late gene expression directs viral DNA replication, structural protein synthesis, and virion assembly. After primary infection of epithelial cells, HSV-1...
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Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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Genital herpes is a sexually transmitted infection primarily caused by herpes simplex virus type 2 (HSV-2), though herpes simplex virus type 1 (HSV-1) is increasingly implicated in genital infections, particularly among younger populations. Transmission occurs mainly through sexual contact, with asymptomatic viral shedding serving as a major route of spread. This characteristic makes HSV-2 difficult to control at a population level, as individuals may unknowingly transmit the virus even in the...
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Cytomegalovirus (CMV) disease is caused by human cytomegalovirus, a double-stranded DNA virus of the Herpesviridae family. While primary CMV infection is often asymptomatic in immunocompetent individuals, the virus can cause severe disease in neonates and immunocompromised patients. CMV is the most common cause of congenital viral infection in the United States, and a major pathogen in solid organ and hematopoietic stem cell transplant recipients.CMV is transmitted via bodily fluids, sexual...

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Related Experiment Video

Updated: Jul 11, 2026

Ex Vivo Infection of Murine Epidermis with Herpes Simplex Virus Type 1
11:56

Ex Vivo Infection of Murine Epidermis with Herpes Simplex Virus Type 1

Published on: August 24, 2015

Evidence for a multiprotein gamma-2 herpesvirus entry complex.

Laurent Gillet1, Philip G Stevenson

  • 1Division of Virology, Department of Pathology, Tennis Court Road, Cambridge CB2 1QP, United Kingdom.

Journal of Virology
|September 28, 2007
PubMed
Summary
This summary is machine-generated.

Murine gammaherpesvirus 68 (MHV-68) uses a complex of glycoproteins for cell entry. The study reveals a core gB/gH complex, with gL and gp150 acting as accessory proteins for epithelial cell adaptation.

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Published on: November 4, 2018

Area of Science:

  • Virology
  • Molecular Biology
  • Cellular Biology

Background:

  • Herpesviruses utilize multiple virion glycoproteins for cellular entry, but their collaborative mechanisms remain unclear.
  • Some glycoproteins may function independently, while others might form a cohesive complex to facilitate viral entry.
  • Murine gammaherpesvirus 68 (MHV-68) entry involves glycoproteins gB, gH, gL, and gp150, with specific roles in binding, fusion, and cell attachment modulation.

Purpose of the Study:

  • To elucidate the complex interactions between MHV-68 virion glycoproteins during cell entry.
  • To determine if glycoproteins form a single complex or act independently.
  • To investigate the roles of gB, gH, gL, and gp150 in the MHV-68 entry pathway.

Main Methods:

  • Coprecipitation assays using glycoprotein-specific antibodies to assess protein associations.
  • Analysis of mutant viruses lacking specific glycoproteins (gp150 and gL) to evaluate their function.
  • In vitro binding assays with B cells and in vivo colonization studies.

Main Results:

  • A gH-specific antibody coprecipitated gB, indicating an association between gH and gB within the virion membrane.
  • A gH/gL-specific antibody also coprecipitated gB, suggesting a tripartite gL/gH/gB complex, though gL was not essential for gH/gB association.
  • gp150 incorporation into virions was partially dependent on gL, implying its contribution to the overall entry complex, while gp150 and gL were not directly bound to gB or gH.
  • Mutants lacking gp150 or both gL and gp150 exhibited enhanced binding to B cells and improved in vivo colonization compared to wild-type MHV-68.

Conclusions:

  • The MHV-68 entry machinery involves a core complex of gB and gH, with gL and gp150 acting as accessory proteins.
  • gp150 and gL appear to facilitate epithelial cell adaptation, enhancing viral entry into specific host cells.
  • Disruption of gp150 leads to increased cell binding, primarily mediated by gB, highlighting the distinct roles of these glycoproteins in the viral entry process.